期刊
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
卷 26, 期 8, 页码 1320-1327出版社
AMER CHEMICAL SOC
DOI: 10.1007/s13361-015-1152-8
关键词
Native mass spectrometry; Proteins; Liquid extraction surface analysis; LESA; Liquid microjunction sampling; Direct surface sampling; Dried blood spots
资金
- EPSRC [EP/L023490/1, EP/K039245/1]
- Birmingham Science City Translational Medicine: Experimental Medicine Network of Excellence Project
- Advantage West Midlands (AWM)
- Engineering and Physical Sciences Research Council [1139522, EP/K039245/1, EP/L023490/1] Funding Source: researchfish
Liquid extraction surface analysis (LESA) mass spectrometry is a promising tool for the analysis of intact proteins from biological substrates. Here, we demonstrate native LESA mass spectrometry of noncovalent protein complexes of myoglobin and hemoglobin from a range of surfaces. Holomyoglobin, in which apomyoglobin is noncovalently bound to the prosthetic heme group, was observed following LESA mass spectrometry of myoglobin dried onto glass and polyvinylidene fluoride surfaces. Tetrameric hemoglobin [(alpha beta)(2) (4H)] was observed following LESA mass spectrometry of hemoglobin dried onto glass and polyvinylidene fluoride (PVDF) surfaces, and from dried blood spots (DBS) on filter paper. Heme-bound dimers and monomers were also observed. The 'contact' LESA approach was particularly suitable for the analysis of hemoglobin tetramers from DBS.
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